Header list of 1zwv.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSFERASE 06-JUN-05 1ZWV
TITLE SOLUTION STRUCTURE OF THE SUBUNIT BINDING DOMAIN (HBSBD) OF THE HUMAN
TITLE 2 MITOCHONDRIAL BRANCHED-CHAIN ALPHA-KETOACID DEHYDROGENASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN
COMPND 3 ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: E1/E3 SUBUNIT BINDING DOMAIN;
COMPND 6 SYNONYM: DIHYDROLIPOYLLYSINE-RESIDUE 2-METHYLPROPANOYL, TRANSFERASE,
COMPND 7 E2, DIHYDROLIPOAMIDE BRANCHED CHAIN TRANSACYLASE, BCKAD E2 SUBUNIT;
COMPND 8 EC: 2.3.1.168;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS SUBUNIT BINDING DOMAIN, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.F.CHANG,D.T.CHUANG,T.H.HUANG
REVDAT 3 02-MAR-22 1ZWV 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1ZWV 1 VERSN
REVDAT 1 21-JUN-05 1ZWV 0
JRNL AUTH C.F.CHANG,D.T.CHUANG,T.H.HUANG
JRNL TITL SOLUTION STRUCTURE OF THE SUBUNIT BINDING DOMAIN (HBSBD) OF
JRNL TITL 2 THE HUMAN MITOCHONDRIAL BRANCHED-CHAIN ALPHA-KETOACID
JRNL TITL 3 DEHYDROGENASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.0
REMARK 3 AUTHORS : PETER GUNTERT
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZWV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000033211.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 295
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : 100MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5MM W/WO U-15N, 13C; 50MM
REMARK 210 PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.1, AURELIA 2.0, CYANA
REMARK 210 2.0
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 HIS A 53
REMARK 465 HIS A 54
REMARK 465 HIS A 55
REMARK 465 HIS A 56
REMARK 465 HIS A 57
REMARK 465 HIS A 58
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 LYS A 24 -169.76 -66.76
REMARK 500 1 LYS A 33 -73.79 -85.16
REMARK 500 1 ILE A 37 88.46 -69.74
REMARK 500 1 THR A 50 63.87 -100.63
REMARK 500 2 ALA A 10 148.04 -178.24
REMARK 500 3 VAL A 29 84.99 -69.59
REMARK 500 3 LYS A 33 -74.29 -87.77
REMARK 500 3 LYS A 48 37.85 -96.17
REMARK 500 4 SER A 26 44.92 -91.87
REMARK 500 4 GLU A 27 -41.12 -147.92
REMARK 500 4 VAL A 29 91.73 -69.33
REMARK 500 4 LYS A 33 -73.34 -82.86
REMARK 500 5 GLU A 2 116.23 -167.28
REMARK 500 5 VAL A 29 85.38 -69.70
REMARK 500 6 VAL A 29 84.72 -69.57
REMARK 500 7 VAL A 29 90.16 -68.97
REMARK 500 7 ASP A 34 53.11 -141.63
REMARK 500 7 ILE A 37 88.40 -68.14
REMARK 500 8 ASN A 22 70.08 54.61
REMARK 500 8 VAL A 29 99.80 -69.25
REMARK 500 8 LYS A 33 -74.67 -85.57
REMARK 500 8 GLN A 49 -70.41 -115.57
REMARK 500 9 LYS A 24 -173.49 -69.96
REMARK 500 9 VAL A 29 85.14 -69.15
REMARK 500 9 LYS A 33 -74.73 -75.30
REMARK 500 10 LYS A 7 174.28 -57.93
REMARK 500 11 LYS A 33 -74.62 -77.43
REMARK 500 12 VAL A 29 85.26 -69.17
REMARK 500 12 LYS A 33 -68.15 -122.00
REMARK 500 12 LYS A 48 38.44 -98.31
REMARK 500 13 ALA A 10 143.54 -173.97
REMARK 500 13 LYS A 33 -75.37 -86.93
REMARK 500 14 VAL A 29 85.36 -69.04
REMARK 500 14 THR A 50 -51.28 -124.42
REMARK 500 14 LEU A 51 172.15 -54.64
REMARK 500 15 ARG A 6 -64.79 -106.10
REMARK 500 15 VAL A 29 84.69 -69.62
REMARK 500 17 VAL A 29 84.78 -69.67
REMARK 500 17 LYS A 48 75.97 37.44
REMARK 500 18 LYS A 33 -75.18 -84.61
REMARK 500 19 LYS A 33 -74.98 -76.81
REMARK 500 20 ILE A 3 44.34 36.81
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1ZWV A 2 50 UNP P11182 ODB2_HUMAN 165 213
SEQADV 1ZWV GLY A 1 UNP P11182 CLONING ARTIFACT
SEQADV 1ZWV LEU A 51 UNP P11182 CLONING ARTIFACT
SEQADV 1ZWV GLU A 52 UNP P11182 CLONING ARTIFACT
SEQADV 1ZWV HIS A 53 UNP P11182 EXPRESSION TAG
SEQADV 1ZWV HIS A 54 UNP P11182 EXPRESSION TAG
SEQADV 1ZWV HIS A 55 UNP P11182 EXPRESSION TAG
SEQADV 1ZWV HIS A 56 UNP P11182 EXPRESSION TAG
SEQADV 1ZWV HIS A 57 UNP P11182 EXPRESSION TAG
SEQADV 1ZWV HIS A 58 UNP P11182 EXPRESSION TAG
SEQRES 1 A 58 GLY GLU ILE LYS GLY ARG LYS THR LEU ALA THR PRO ALA
SEQRES 2 A 58 VAL ARG ARG LEU ALA MET GLU ASN ASN ILE LYS LEU SER
SEQRES 3 A 58 GLU VAL VAL GLY SER GLY LYS ASP GLY ARG ILE LEU LYS
SEQRES 4 A 58 GLU ASP ILE LEU ASN TYR LEU GLU LYS GLN THR LEU GLU
SEQRES 5 A 58 HIS HIS HIS HIS HIS HIS
HELIX 1 1 THR A 11 ASN A 21 1 11
HELIX 2 2 LEU A 38 LYS A 48 1 11
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - r 2 2 Bytes